Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016298 | molecular_function | lipase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0008203 | biological_process | cholesterol metabolic process |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016298 | molecular_function | lipase activity |
| B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PROSITE/UniProt
| site_id | PS01173 |
| Number of Residues | 17 |
| Details | LIPASE_GDXG_HIS Lipolytic enzymes "G-D-X-G" family, putative histidine active site. IVhFHGGGFvaqTsrSH |
| Chain | Residue | Details |
| A | ILE346-HIS362 | |
| site_id | PS01174 |
| Number of Residues | 13 |
| Details | LIPASE_GDXG_SER Lipolytic enzymes "G-D-X-G" family, putative serine active site. IcLAGDSAGGnLC |
| Chain | Residue | Details |
| A | ILE418-CYS430 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole","evidences":[{"source":"UniProtKB","id":"Q5NUF3","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q8BLF1","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU10038","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q8BLF1","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P15304","evidenceCode":"ECO:0000250"}]} |